ID   GS18_BACSU              Reviewed;         172 AA.
AC   P80876;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=General stress protein 18;
DE            Short=GSP18;
DE            EC=3.2.-.-;
GN   Name=yfkM; OrderedLocusNames=BSU07850;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   PubMed=8969503; DOI=10.1099/13500872-142-11-3057;
RA   Yamamoto H., Uchiyama S., Sekiguchi J.;
RT   "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees
RT   region of the Bacillus subtilis chromosome containing genes for trehalose
RT   metabolism and acetoin utilization.";
RL   Microbiology 142:3057-3065(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-30.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=19170879; DOI=10.1111/j.1365-2958.2008.06568.x;
RA   Nguyen T.T.H., Eiamphungporn W., Maeder U., Liebeke M., Lalk M., Hecker M.,
RA   Helmann J.D., Antelmann H.;
RT   "Genome-wide responses to carbonyl electrophiles in Bacillus subtilis:
RT   control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine
RT   proteinase YraA by the MerR-family regulator YraB (AdhR).";
RL   Mol. Microbiol. 71:876-894(2009).
CC   -!- FUNCTION: Functions in the protection against aldehyde-stress, possibly
CC       by degrading damaged proteins. {ECO:0000269|PubMed:19170879}.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation and oxygen limitation.
CC   -!- DISRUPTION PHENOTYPE: When combined with a yraA disruption shows
CC       significantly reduced growth in the presence of formaldehye and
CC       methylglyoxal. {ECO:0000269|PubMed:19170879}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
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DR   EMBL; D83967; BAA23403.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12614.1; -; Genomic_DNA.
DR   PIR; H69808; H69808.
DR   RefSeq; NP_388666.1; NC_000964.3.
DR   RefSeq; WP_003243504.1; NZ_JNCM01000032.1.
DR   AlphaFoldDB; P80876; -.
DR   SMR; P80876; -.
DR   STRING; 224308.BSU07850; -.
DR   MEROPS; C56.001; -.
DR   PaxDb; P80876; -.
DR   PRIDE; P80876; -.
DR   EnsemblBacteria; CAB12614; CAB12614; BSU_07850.
DR   GeneID; 938808; -.
DR   KEGG; bsu:BSU07850; -.
DR   PATRIC; fig|224308.179.peg.849; -.
DR   eggNOG; COG0693; Bacteria.
DR   InParanoid; P80876; -.
DR   OMA; YAWMREF; -.
DR   PhylomeDB; P80876; -.
DR   BioCyc; BSUB:BSU07850-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR006286; C56_PfpI.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42733; PTHR42733; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01382; PfpI; 1.
DR   PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Protease; Reference proteome;
KW   Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298659"
FT   CHAIN           2..172
FT                   /note="General stress protein 18"
FT                   /id="PRO_0000157832"
FT   DOMAIN          3..171
FT                   /note="PfpI endopeptidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
SQ   SEQUENCE   172 AA;  18863 MW;  DA183A4EE10BEB1E CRC64;
     MGKKIAVVLT YYFEDSEYTE PAKAFKEAGH ELTVIEKEKG KTVKGKQGTA EVTVDASIDD
     VNSSDFDALL IPGGFSPDQL RADDRFVQFT KAFMTDKKPV FAICHGPQLL INAKALDGRK
     ATGYTSIRVD MENAGADVVD KEVVVCQDQL VTSRTPDDIP AFNRESLALL EK